Protein O-GlcNAcylation: emerging mechanisms and functions

By Xiaoyong Yang, Kevin Qian. Nature reviews. Molecular cell biology, 2017

1,074 citations recorded by the source corpus.

O-GlcNAcylation — the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins — is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes — O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) — controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood.

Subfields: Immunology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/b3a5044bbe1ed4980b105492cc9da1b2e2fbb2c0

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In Molecular Biology

1. Ping Gao
2. Huafeng Zhang
3. Linchong Sun

Citations in the corpus

• Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “…GlcNAc), the final product of the hexosamine biosynthetic pathway (HBP) that integrates glucose, glutamine, amino acid, fatty acid, and nucleotide metabolism, serves as the donor substrate for OGlcNAcylation (Hart et al., 2007; Hart et al., 2011; Ferrer et al., 2016; Yang and Qian, 2017) (Fig.”